Aldehyde oxidases of Drosophila: contributions of several enzymes to observed activity patterns.
At least four enzymes contribute to histochemically, electrophoretically, or spectrophotometrically detectable aldehyde oxidase (AO) activity in Drosophila melanogaster. The one we designate AO-1 contributes the majority of activity measured in extracts of whole flies. Pyridoxal oxidase (PO) is also a broad range AO. It is prominent only in midgut and Malpighian tubules, where it apparently accounts for a substantial fraction of total AO activity. The tissue distributions of these enzymes are clearly disparate despite close linkage of their structural loci and parallel dependence on the mal, lxd, and cin loci. A similarly related enzyme, xanthine dehydrogenase (XDH), is detected as an AO only in electrophoretic gels. A fourth broad range AO, not dependent on mal, lxd, and cin, is confined to the ejaculatory bulb. A similar array of AO isozymes is present in phylogenetically distant Drosophila species.
D042931:Aldehyde Oxidase; D000445:Aldehyde Oxidoreductases / Q000235:genetics*; D000818:Animals; D000906:Antibodies; D004331:Drosophila melanogaster / Q000201:enzymology / Q000235:genetics*; D005260:Female; D005796:Genes; D008040:Genetic Linkage; D007118:Immunoassay; D007527:Isoenzymes / Q000235:genetics*; D009154:Mutation; D009928:Organ Specificity; D010641:Phenotype; D013379:Substrate Specificity
D000906:Antibodies; D007527:Isoenzymes; D000445:Aldehyde Oxidoreductases; D042931:Aldehyde Oxidase